3HLI
diisopropyl fluorophosphatase (DFPase), active site mutants
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005509 | molecular_function | calcium ion binding |
A | 0008150 | biological_process | biological_process |
A | 0016787 | molecular_function | hydrolase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0047862 | molecular_function | diisopropyl-fluorophosphatase activity |
B | 0005509 | molecular_function | calcium ion binding |
B | 0008150 | biological_process | biological_process |
B | 0016787 | molecular_function | hydrolase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0047862 | molecular_function | diisopropyl-fluorophosphatase activity |
C | 0005509 | molecular_function | calcium ion binding |
C | 0008150 | biological_process | biological_process |
C | 0016787 | molecular_function | hydrolase activity |
C | 0046872 | molecular_function | metal ion binding |
C | 0047862 | molecular_function | diisopropyl-fluorophosphatase activity |
D | 0005509 | molecular_function | calcium ion binding |
D | 0008150 | biological_process | biological_process |
D | 0016787 | molecular_function | hydrolase activity |
D | 0046872 | molecular_function | metal ion binding |
D | 0047862 | molecular_function | diisopropyl-fluorophosphatase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 315 |
Chain | Residue |
A | GLU21 |
A | ASN120 |
A | ASN175 |
A | ASP229 |
A | HOH318 |
A | HOH319 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 316 |
Chain | Residue |
A | HOH321 |
A | HOH325 |
A | HOH328 |
A | ASP232 |
A | LEU273 |
A | HIS274 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA B 315 |
Chain | Residue |
A | PHE314 |
B | GLU21 |
B | ASN120 |
B | ASN175 |
B | ASP229 |
B | HOH324 |
B | HOH369 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 316 |
Chain | Residue |
B | ASP232 |
B | LEU273 |
B | HIS274 |
B | HOH338 |
B | HOH367 |
B | HOH378 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA C 315 |
Chain | Residue |
B | PHE314 |
C | GLU21 |
C | ASN120 |
C | ASN175 |
C | ASP229 |
C | HOH317 |
C | HOH320 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA C 316 |
Chain | Residue |
C | ASP232 |
C | LEU273 |
C | HIS274 |
C | HOH318 |
C | HOH319 |
C | HOH330 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA D 315 |
Chain | Residue |
D | GLU21 |
D | ASN120 |
D | ASN175 |
D | ASP229 |
D | HOH317 |
D | HOH326 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA D 316 |
Chain | Residue |
D | ASP232 |
D | LEU273 |
D | HIS274 |
D | HOH318 |
D | HOH321 |
D | HOH329 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:15966726 |
Chain | Residue | Details |
A | HIS287 | |
B | HIS287 | |
C | HIS287 | |
D | HIS287 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000305 |
Chain | Residue | Details |
A | GLU21 | |
C | ASN120 | |
C | ASN175 | |
C | ASP229 | |
D | GLU21 | |
D | ASN120 | |
D | ASN175 | |
D | ASP229 | |
A | ASN120 | |
A | ASN175 | |
A | ASP229 | |
B | GLU21 | |
B | ASN120 | |
B | ASN175 | |
B | ASP229 | |
C | GLU21 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11435114, ECO:0000269|PubMed:14501113 |
Chain | Residue | Details |
A | ASP232 | |
D | ASP232 | |
D | LEU273 | |
D | HIS274 | |
A | LEU273 | |
A | HIS274 | |
B | ASP232 | |
B | LEU273 | |
B | HIS274 | |
C | ASP232 | |
C | LEU273 | |
C | HIS274 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1e1a |
Chain | Residue | Details |
A | HIS287 | |
A | ASP37 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1e1a |
Chain | Residue | Details |
B | HIS287 | |
B | ASP37 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1e1a |
Chain | Residue | Details |
C | HIS287 | |
C | ASP37 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1e1a |
Chain | Residue | Details |
D | HIS287 | |
D | ASP37 |
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 686 |
Chain | Residue | Details |
A | GLU21 | increase nucleophilicity, metal ligand, proton acceptor |
A | ASP37 | electrostatic stabiliser, increase basicity |
A | ASN120 | metal ligand |
A | ASN175 | metal ligand |
A | ASP229 | covalently attached, electrofuge, electrophile, increase nucleophilicity, metal ligand, nucleophile, proton acceptor |
A | HIS287 | increase nucleophilicity, proton acceptor |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 686 |
Chain | Residue | Details |
B | GLU21 | increase nucleophilicity, metal ligand, proton acceptor |
B | ASP37 | electrostatic stabiliser, increase basicity |
B | ASN120 | metal ligand |
B | ASN175 | metal ligand |
B | ASP229 | covalently attached, electrofuge, electrophile, increase nucleophilicity, metal ligand, nucleophile, proton acceptor |
B | HIS287 | increase nucleophilicity, proton acceptor |
site_id | MCSA3 |
Number of Residues | 6 |
Details | M-CSA 686 |
Chain | Residue | Details |
C | GLU21 | increase nucleophilicity, metal ligand, proton acceptor |
C | ASP37 | electrostatic stabiliser, increase basicity |
C | ASN120 | metal ligand |
C | ASN175 | metal ligand |
C | ASP229 | covalently attached, electrofuge, electrophile, increase nucleophilicity, metal ligand, nucleophile, proton acceptor |
C | HIS287 | increase nucleophilicity, proton acceptor |
site_id | MCSA4 |
Number of Residues | 6 |
Details | M-CSA 686 |
Chain | Residue | Details |
D | GLU21 | increase nucleophilicity, metal ligand, proton acceptor |
D | ASP37 | electrostatic stabiliser, increase basicity |
D | ASN120 | metal ligand |
D | ASN175 | metal ligand |
D | ASP229 | covalently attached, electrofuge, electrophile, increase nucleophilicity, metal ligand, nucleophile, proton acceptor |
D | HIS287 | increase nucleophilicity, proton acceptor |